The TRPM7 channel is inactivated by PIP2 hydrolysis

Loren W. Runnels, Lixia Yue, David E. Clapham

Research output: Contribution to journalArticle

416 Scopus citations

Abstract

TRPM7 (ChaK1, TRP-PLIK, LTRPC7) is a ubiquitous, calcium-permeant ion channel that is unique in being both an ion channel and a serine/threonine kinase. The kinase domain of TRPM7 directly associates with the C2 domain of phospholipase C (PLC). Here, we show that in native cardiac cells and heterologous expression systems, Gαq-linked receptors or tyrosine kinase receptors that activate PLC potently inhibit channel activity. Numerous experimental approaches demonstrated that phosphatidylinositol 4,5-bisphosphate (PIP2), the substrate of PLC, is a key regulator of TRPM7. We conclude that receptor-mediated activation of PLC results in the hydrolysis of localized PIP2, leading to inactivation of the TRPM7 channel.

Original languageEnglish (US)
Pages (from-to)329-336
Number of pages8
JournalNature cell biology
Volume4
Issue number5
DOIs
StatePublished - May 27 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Cell Biology

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